2.3.1.165	C216A	mutant without catalytic activity	703206	
2.3.1.165	H939A	mutant with catalytic activity	703206	
2.3.1.165	H958A	mutation in the THID active site	735433	
2.3.1.165	H972A	site-directed mutagenesis, the reaction intermediate is bound to the thioester hydrolase domain of ATX formed in the presence of NADPH, and is released as 6-methylsalicylic acid by both the intact ATX and by truncated THID mutant in trans	719864	
2.3.1.165	additional information	aomsas disruption mutants are not able to produce 6-methylsalicylic acid, isoasperlactone and asperlactone	703824	
2.3.1.165	additional information	construction of the THID mutant protein, a His-tagged 61 kDA 541-amino acid region containing thioester hydrolase domain and its downstream, THID shows catalytic activity to hydrolyze a model substrate 6-methylsalicylic acid-N-acetylcysteamine. The complementation of thioester domain-deficient mutant THm by THID protein in the recombinant Escherichia coli expression system	719864	
2.3.1.165	additional information	deletion of one of the 6-methylsalicylic acid synthase domains ketosynthase, acyltransferase, dehydratase, ketoreductase, or acyl carrier protein results in a lost of catalytic activity	703206	
2.3.1.165	additional information	N-terminal deletion mutant ATXN1 lacking 44 amino acids, catalytically active. N-terminal deletion mutant ATXN2 lacking 81 amino acids including part of the ketosynthase domain, loss of catalytic activity. Both ATXC1 lacking 9 carboxyterminal amino acids and ATXC2 lacking 21 carboxyterminal amino acids including part of the conserved acyl carrier protein domain are inactive. Coexpression of inactive mutants ATXN2 with ATXC1 or ATXC2 results in restauration of activity. Identification of an interdomain region required for the formation of the active reaction center	673079	
2.3.1.165	additional information	Saccharomyces cerevisiae strain IBT100083 with a ACC1-TEF1 promoter produces high levels of acetyl-CoA carboxylase (ACC1) which catalyzes the conversion of acetyl-CoA to malonyl-CoA. Hence, more substrate for 6-methylsalicylic acid synthase is available resulting in a higher 6-MSA production.	705512	
2.3.1.165	S1761A	mutant without catalytic activity	703206	
2.3.1.165	S667A	mutant without catalytic activity	703206